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| | <StructureSection load='3hs2' size='340' side='right'caption='[[3hs2]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3hs2' size='340' side='right'caption='[[3hs2]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hs2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp1 Bpp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HS2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hs2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P1 Escherichia virus P1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HS2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hry|3hry]], [[3dd7|3dd7]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phd ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10678 BPP1])</td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hs2 OCA], [https://pdbe.org/3hs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hs2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hs2 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hs2 OCA], [https://pdbe.org/3hs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hs2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hs2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHD_BPP1 PHD_BPP1]] Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that binds to the doc toxin and neutralizes its toxic effect. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid. Phd and doc proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss.<ref>PMID:9829946</ref> <ref>PMID:18398006</ref> Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression.<ref>PMID:9829946</ref> <ref>PMID:18398006</ref>
| + | [https://www.uniprot.org/uniprot/PHD_BPP1 PHD_BPP1] Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that binds to the doc toxin and neutralizes its toxic effect. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid. Phd and doc proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss.<ref>PMID:9829946</ref> <ref>PMID:18398006</ref> Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression.<ref>PMID:9829946</ref> <ref>PMID:18398006</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpp1]] | + | [[Category: Escherichia virus P1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garcia-Pino, A]] | + | [[Category: Garcia-Pino A]] |
| - | [[Category: Loris, R]] | + | [[Category: Loris R]] |
| - | [[Category: Antitoxin]]
| + | |
| - | [[Category: Doc]]
| + | |
| - | [[Category: Intrinsic disorder]]
| + | |
| - | [[Category: Phd]]
| + | |
| - | [[Category: Prevent host death]]
| + | |
| - | [[Category: Toxin-antitoxin]]
| + | |
| Structural highlights
Function
PHD_BPP1 Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that binds to the doc toxin and neutralizes its toxic effect. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid. Phd and doc proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss.[1] [2] Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression.[3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Regulation of the phd/doc toxin-antitoxin operon involves the toxin Doc as co- or derepressor depending on the ratio between Phd and Doc, a phenomenon known as conditional cooperativity. The mechanism underlying this observed behavior is not understood. Here we show that monomeric Doc engages two Phd dimers on two unrelated binding sites. The binding of Doc to the intrinsically disordered C-terminal domain of Phd structures its N-terminal DNA-binding domain, illustrating allosteric coupling between highly disordered and highly unstable domains. This allosteric effect also couples Doc neutralization to the conditional regulation of transcription. In this way, higher levels of Doc tighten repression up to a point where the accumulation of toxin triggers the production of Phd to counteract its action. Our experiments provide the basis for understanding the mechanism of conditional cooperative regulation of transcription typical of toxin-antitoxin modules. This model may be applicable for the regulation of other biological systems.
Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity.,Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R Cell. 2010 Jul 9;142(1):101-11. PMID:20603017[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Magnuson R, Yarmolinsky MB. Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol. 1998 Dec;180(23):6342-51. PMID:9829946
- ↑ Liu M, Zhang Y, Inouye M, Woychik NA. Bacterial addiction module toxin Doc inhibits translation elongation through its association with the 30S ribosomal subunit. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5885-90. doi:, 10.1073/pnas.0711949105. Epub 2008 Apr 8. PMID:18398006 doi:10.1073/pnas.0711949105
- ↑ Magnuson R, Yarmolinsky MB. Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol. 1998 Dec;180(23):6342-51. PMID:9829946
- ↑ Liu M, Zhang Y, Inouye M, Woychik NA. Bacterial addiction module toxin Doc inhibits translation elongation through its association with the 30S ribosomal subunit. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5885-90. doi:, 10.1073/pnas.0711949105. Epub 2008 Apr 8. PMID:18398006 doi:10.1073/pnas.0711949105
- ↑ Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell. 2010 Jul 9;142(1):101-11. PMID:20603017 doi:10.1016/j.cell.2010.05.039
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